Developments in Biotechnological Research in Austria

References

• Röhr M., Kominek J., Kubicek C. P. Organic acids and other small molecules. Aspergillus: The Biology and Industrial Application, J. W. Bennett, M. Klich. Butterworth Publishers, Stoneham, MA 1991; 91
   Google Scholar
• Xu D. B., Röhr M., Kubicek C. P. A comparison of factors influencing citric acid production by Aspergillus niger in submerged culture and on filter paper discs. Appl. Microbiol. Biotechnol. 1989; 30: 444
   Web of Science ®Google Scholar
• Xu D. B., Madrid C. P., Röhr M., Kubicek C. P. The influence of type and concentration of the carbon source on the production of citric acid by. Aspergillus niger. Appl. Microbiol. Biotechnol. 1989; 30: 553
   Web of Science ®Google Scholar
• Schreferl-Kunar G., Grotz M., Röhr M., Kubicek C. P. Citric acid production by Aspergillus niger mutants with increased glycolytic capacity. FEMS Microbiol. Lett. 1989; 59: 297
   Web of Science ®Google Scholar
• Steinböck F. A., Held I., Choojun S., Harmsen H., Röhr M., Kubicek-Pranz E. M., Kubicek C. P. Regulatory aspects of carbohydrate metabolism in relation to citric acid accumulation by. Aspergillus niger. Acta Biotechnol. 1991; 11: 571
   Google Scholar
• Kubicek-Pranz E. M., Mozelt M., Röhr M., Kubicek C. P. Changes in the concentration of fructose-2,6-bisphosphate in Aspergillus niger during stimulation of acidogenesis by elevated sucrose concentrations. Biochim. Biophys. Acta 1990; 1033: 250
   PubMed Web of Science ®Google Scholar
• Harmsen H. J. M., Kubicek-Pranz E. M., Röhr M., Visser J., Kubicek C. P. Regulation of 6-phosphofructo-2-kinase from the citric acid accumulating fungus. Aspergillus niger. Appl. Microbiol. Biotechnol. 1992; 37: 784
   Web of Science ®Google Scholar
• Steinböck F., Choojun S., Held I., Roehr M., Kubicek C. P. Characterization and regulatory properties of a single hexokinase from the citric acid accumulating fungus. Aspergillus niger. Biochim. Biophys. Acta 1994; 1200: 215
   PubMed Web of Science ®Google Scholar
• Torres N. V., Riol-Cimas J. M., Wolschek M., Kubicek C. P. Glucose transport by Aspergillus niger: the low affinity carrier is only formed during growth on high glucose concentrations. Appl. Microbiol. Biotechnol. 1996; 44: 790
   Google Scholar
• Wolschek M., Kubicek C. P. Cloning and characterization of the tpsl (trehalose-6-phosphate subunit-1 encoding) gene of Aspergillus niger. 7th Int. Symp. Genet. Ind. Microorg. (GIM94), Abstract
   Google Scholar
• Kubicek C. P. The role of the citric acid cycle in fungal organic acid fermentations. Biochem. Soc. Symp., 54: 113–126
   PubMedGoogle Scholar
• Jaklitsch W. M., Kubicek C. P., Scrutton M. C. Intracellular organisation of citrate production in. Aspergillus niger. Can. J. Microbiol. 1991; 37: 823
   PubMedGoogle Scholar
• Jaklitsch W. M., Kubicek C. P., Scrutton M. C. Subcellular localization of enzymes of itaconate biosynthesis in. Aspergillus terreus. J. Gen. Microbiol. 1991; 137: 533
   Google Scholar
• Kubicek C. P., Schreferl-Kunar G., Wöhrer W., Röhr M. Evidence for a cytoplasmic pathway of oxalate biosynthesis in Aspergillus niger. Appl. Environ. Microbiol., 54: 633–637
   PubMedGoogle Scholar
• Jaklitsch W. M., Hampel W., Röhr M., Kubicek C. P., Gamerith G. α-Aminoadipate pool concentration and penicillin biosynthesis in strains of Penicillium chrysogenum. Can. J. Microbiol. 1986; 32: 473
   PubMedGoogle Scholar
• Hönlinger C., Kubicek C. P. Regulation of δ-(l-α-aminoadipyl)-l-cysteinyl-valine and isopenicillin N biosynthesis in Penicillium chrysogenum by the α-aminoadipate pool size. FEMS Microbiol. Lett. 1989; 65: 71
   Google Scholar
• Jaklitsch W. M., Kubicek C. P. Homocitrate synthase from Penicillium chrysogenum: subcellular localization, purification of the cytosolic isoenzyme and sensitivity to lysine. Biochem. J. 1990; 269: 247
   PubMedGoogle Scholar
• Affenzeller K., Hönlinger C., Jaklitsch W. M., Kubicek C. P. Lysine biosynthesis in Penicillium chrysogenum is regulated by feedback inhibition of α-aminoadipate reductase. FEMS Microbiol. Lett. 1988; 58: 293
   Google Scholar
• Lu Y., Mach R. L., Affenzeller K. M., Kubicek C. P. Regulation of α-aminoadipate reductase from Penicillium chrysogenum in relation to the flux from α-aminoadipate into penicillin biosynthesis. Can. J. Microbiol. 1992; 38: 758
   PubMedGoogle Scholar
• Kubicek C. P., Hönlinger C., Jaklitsch W. M., Affenzeller K., Mach R., Gerngrob T.-U., Lu Y. Regulation of lysine biosynthesis in the fungus Penicillium chrysogenum. Amino Acids: Chemistry, Biology and Medicine, G. Lubec, G. A. Rosenthal. Escom, LeidenNetherlands 1992; 1029
   Google Scholar
• Hönlinger C., Kubicek C. P. Metabolism and compartmentation of α-aminoadipate in penicillium producing strains of. Penicillium chrysogenum. Biochim. Biophys. Acta 1989; 993: 204
   Google Scholar
• Affenzeller K., Kubicek C. P. Evidence for a compartmentation of amino acids in penicillin biosynthesis in Penicillium chrysogenum strains. J. Gen. Microbiol. 1991; 137: 1655
   Google Scholar
• Lendenfeld T., Ghali D., Wolschek M., Kubicek-Pranz E. M., Kubicek C. P. Subcellular compartmentation of penicillin biosynthesis in Penicillium chrysogenum. The amino acid precursors are derived from the vacuole. J. Biol. Chem., 268: 665–671
   PubMedGoogle Scholar
• Kolar M., Holzmann K., Weber G., Leitner E., Schwab H. Molecular characterization and functional analysis in Aspergillus nidulans of the 5′ region of the Penicillium chrysogenum isopenicillin N synthetase gene. J. Biotechnol. 1991; 17: 67
   PubMedGoogle Scholar
• Feng B., Friedlin E., Marzluf G. A. A reporter gene analysis of penicillin biosynthesis gene expression in Penicillium chrysogenum and its regulation by nitrogen and glucose catabolite repression. Appl. Environ. Microbiol. 1994; 60: 4432
   PubMedGoogle Scholar
• Feng B., Friedlin E., Marzluf G. A. Nuclear DNA-binding proteins which recognize the intergenic control region of penicillin biosynthetic genes. Curr. Genet. 1995; 27: 351
   PubMedGoogle Scholar
• Haas H., Bauer B., Redl B., Stöffler G., Marzluf G. A. Molecular cloning and analysis of nre, the major nitrogen regulatory gene of. Penicillium chrysogenum. Curr. Genet. 1995; 27: 150
   PubMedGoogle Scholar
• Haas H., Redl B., Friedlin E., Stöffler G. Isolation and analysis of the Penicillium chrysogenum phoA gene encoding a secreted phosphate-repressible acid phosphatase. Gene 1992; 113: 129
   PubMed Web of Science ®Google Scholar
• Haas H., Friedlin E., Stöffler G., Redl B. Cloning and structural organization of a xylanase-encoding gene from. Penicillium chrysogenum. Gene 1993; 126: 237
   PubMedGoogle Scholar
• Graessle S., Haas H., Redl B., Friedlin E., Kuerasteiner H., Stoeffler G. Expression of cloned genes in Penicillium chrysogenum. 18th Fungal Genetics Conf. March. Asilomar, 1995; 1–31
   Google Scholar
• Schreiner E., Holzmann K., Schwab H. Characterization of the specifically regulated aox-gene of Penicillium chrysogenum. 18th Fungal Genetics Conf. March. Asilomar, 1995; iii–3
   Google Scholar
• Weber G., Schörgendorfer K., Schneider-Scherzer E., Leitner E. The peptide synthetase catalyzing cyclosporin production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame. Curr. Genet. 1994; 26: 120
   PubMedGoogle Scholar
• Leitner E., Schneider E., Schörgendorfer K., Weber G., European Patent Appl. 0578616, (Sandoz Ltd.)
   Google Scholar
• , Reference deleted
   Google Scholar
• Kalousek S., Schrot G., Lubitz H. W. Expression of the Alkaligenes eutrophus phbA gene in Escherichia coli using a positive selection vector based on phage Lambda cell lysis. J. Biotechnol. 1994; 33: 15
   PubMedGoogle Scholar
• Steiner W., Lafferty R. M., Gomes I., Esterbauer H. Studies on a wild-strain of Schizophyllum commune: cellulase and xylanase production and formation of an extracellular polysaccharide schizophyllan. Biotechnol. Bioeng. 1987; 30: 169
   PubMed Web of Science ®Google Scholar
• Sleytr U. B., Sara M., Messner P., Pum D. Application potential of 2D protein crystals (S-layers). Ann. N.Y. Acad. Sci. 1995
   Google Scholar
• Messner P., Sleytr U. B. Crystalline bacterial cell surface layers. Adv. Microb. Physiol. 1992; 33: 213
   PubMedGoogle Scholar
• Sara M., Sleytr U. B. Production and characteristics of ultrafiltration membranes with uniform pores from two-dimensional arrays of proteins. J. Membr. Sci. 1987; 33: 27
   Google Scholar
• Sara M., Sleytr U. B. Membrane biotechnology: two-dimensional protein crystals for ultrafiltration purposes. Biotechnology, H. J. Rehm, 1988; Vol. 6b: 615
   Google Scholar
• Sara M., Sleytr U. B. Molecular sieving through S-layers of Bacillus stearothermophilus strains. J. Bacteriol. 1987; 169: 4092
   PubMedGoogle Scholar
• Sleytr U. B., Sara M. Use of a Structure with Membranes Having Continuous Pores. U.S. Patent 4,849,109., 1989
   Google Scholar
• Sleytr U. B., Sara M. Structure with Membranes Having Continuous Pores. U.S. Patent 4,886,604, 1989
   Google Scholar
• Küpcü S., Sara M., Sleytr U. B. Influence of covalent attachment of low molecular weight substances on the rejection and absorption properties of crystalline proteinaceous ultrafiltration membranes. Desalination 1993; 90: 65
   Google Scholar
• Sara M., Küpcü S., Weiner C., Weigert S., Sleytr U. B. Crystalline protein layers as isoporous molecular sieves and immobilization and affinity matrices. Immobilized Macromolecules: Application Potentials, U. B. Sleytr, et al, 1993; 71
   Google Scholar
• Sara M., Pum D., Sleytr U. B. Permeability and charge-dependent adsorption properties of the S-layer lattice from Bacillus coagulans E38-66. J. Bacteriol. 1992; 174: 3487
   PubMedGoogle Scholar
• Sara M., Küpcü S., Weiner C., Weigert S., Sleytr U. B. S-layers as immobilization and affinity matrix. Advances in Bacterial Paracrystalline Surface Layers, T. J. Beveridge, S. F. Koval, 1993; 204
   Google Scholar
• Weiner C., Sara M., Sleytr U. B. Novel protein A affinity matrices prepared from two-dimensional protein crystals. Biotechnol. Bioeng. 1994; 43: 321
   PubMedGoogle Scholar
• Neubauer A., Pum D., Sleytr U. B. An amperometric glucose sensor based on isoporous crystalline protein membranes as immobilization matrix. Anal. Lett. 1993; 26: 1347
   Web of Science ®Google Scholar
• Neubauer A., Hödl C., Pum D., Sleytr U. B. A multistep enzyme sensor for sucrose based on S-layer microparticles as immobilization matrix. Anal. Lett. 1994; 27: 849
   Web of Science ®Google Scholar
• Pum D., Sleytr U. B. Molecular nanotechnology with S-layers. Advances in Bacterial Paracrystalline Surface Layers, T. J. Beveridge, S. F. Koval, 1993; 195
   Google Scholar
• Malcolm A. J., Messner P., Sleytr U. B., Smith R. H., Unger F. M. Crystalline bacterial cell surface layers (S-layers) as combined carrier/adjuvants for conjugate vaccines. Immobilized Macromolecules: Application Potentials, U. B. Sleytr, et al, 1993; 195
   Google Scholar
• Malcolm A. J., Best M. W., Szarka R. J., Mosleh Z., Unger F. M., Messner P. Surface layers from Bacillus alvei as a carrier for a Streptococcus pneumoniae conjugate vaccine. Advances in Bacterial Paracrystalline Surface Layers, T. J. Beveridge, S. F. Koval, 1993; 219
   Google Scholar
• Sleytr U. B., Mundt W., Messner P. Immunogenic compositions containing ordered carriers. U.S. Patent 5,043,158, 1991
   Google Scholar
• Messner P., Mazid M. A., Unger F. M., Sleytr U. B. Artificial antigens. Synthetic carbohydrate haptens immobilized on crystalline bacterial surface layer glycoproteins. Carbohydr. Res. 1992; 233: 175
   PubMedGoogle Scholar
• Sleytr U. B., Mundt W., Messner P. Pharmazeutische Struktur mit an Proteinträgern gebundenen Wirkstoffen. European Patent No. 0306473, 1993
   Google Scholar
• Smith R. H., Messner P., Lamontage R. L., Sleytr U. B., Unger F. M. Induction of T-cell immunity to oligosaccharide antigens immobilized on crystalline bacterial surface layers (S-layers). Vaccine 1993; 11: 919
   PubMedGoogle Scholar
• Sleytr U. B., Messner P. Crystalline surface layers in prokaryotes. J. Bacteriol. 1988; 170: 2891
   PubMedGoogle Scholar
• Pum D., Weinhandl M., Hödl C., Sleytr U. B. Large-scale crystallisation of the S-layer of Bacillus coagulans E38-66 at the air/water interface and on lipid films. J. Bacteriol. 1993; 175: 2762
   PubMedGoogle Scholar
• Pum D., Sleytr U. B. Large scale reconstitution of crystalline bacterial surface layer (S-layer) proteins at the air/water interface and on lipid films. Thin Solid Films 1994; 244: 882
   Google Scholar
• Pum D., Hödl C., Neubauer A., Kainz U., Schreier W., Sara M., Sleytr U. B. Use of crystalline bacterial cell-surface layers (S-layers) for the development of bioanalytical sensors. GBF-Monograph, F. Scheller, R. D. Schmid, 1991; Vol. 17: 535
   Google Scholar
• Pum D., Sara M., Messner P., Sleytr U. B. Two-dimensional (glyco) protein crystals as pattering elements for the controlled immobilization of functional molecules. Nanotechnology 1991; 2: 196
   Google Scholar
• Taga K., Kellner R., Kainz U., Sleytr U. B. In situ attenuated total reflectance FT-IR analysis of an enzyme-modified mid-infrared fiber surface using crystalline bacterial surface proteins. Anal. Chem. 1994; 66: 35
   Google Scholar
• Kuen B., Sleytr U. B., Lubitz W. Sequence analysis of the sbs A gene encoding the 130-kDa surface layer protein of Bacillus stearothermophilus strain PV72. Gene 1993; 145: 115
   Google Scholar
• Kuen B., Lubitz H. W., Sara M., Sleytr U. B. S-layer of Bacillus stearothermophilus PV72. Immobilized Macromolecules: Application Potentials, U. B. Sleytr, et al. Springer, London 1993; 303
   Google Scholar
• Kubicek C. P., Eveleigh D. E., Esterbauer H., Steiner W., Kubicek-Pranz E. M. Trichoderma Cellulases: Biochemistry, Physiology, Genetics and Applications. Royal Chemical Society Press, Cambridge
   Google Scholar
• Esterbauer H., Steiner W., Kreiner W., Sattler W., Hayn M. Comparison of enzymatic hydrolysis in a world-wide round robin assay. Bioresour. Technol. 1992; 39: 117
   Google Scholar
• Chen H., Hayn M., Esterbauer H. Three forms of cellobiohydrolase I from. Trichoderma reesei. Biochem. Mol. Biol. Inter. 1993; 30: 901
   PubMedGoogle Scholar
• Nidetzky B., Steiner W. A new approach for modelling cellulase-cellulose adsorption and the kinetics of the enzymatic hydrolysis of microcrystalline cellulose. Biotechnol. Bioeng. 1993; 42: 469
   PubMed Web of Science ®Google Scholar
• Nidetzky B., Steiner W., Claeyssens M. Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of the two cellobiohydrolases, two endocellulases and their core proteins on filter paper and their relation to hydrolysis. Biochem. J. 1994; 303: 817
   PubMed Web of Science ®Google Scholar
• Hayn M., Klinger R., Esterbauer H. Isolation and partial characterization of a low-molecular weight endoglucanase from Trichoderma reesei. Proc. Second TRICEL Symp. Trichoderma reesei Cellulases and Other Hydrolytic Enzymes, P. Suominen, T. Reinikainen. Foundation of Biotechnical and Industrial Fermentation Research, EspooFinland 1993; 147
   Google Scholar
• Chen H., Hayn M., Esterbauer H. Purification and characterization of two extracellular β-glucosidases from. Trichoderma reesei. Biochim. Biophys. Acta 1992; 1121: 54
   PubMed Web of Science ®Google Scholar
• Mach R. L., Seiboth B., Myasnikov A., Gonzalez R., Strauss J., Harkki A. M., Kubicek C. P. The bgl1 gene of Trichoderma reesei QM 9414 encodes an extracellular, cellulose-inducible β-glucosidase involved in cellulase induction by sophorose. Mol. Microbiol., 16: 687
   PubMedGoogle Scholar
• Mischak H., Hofer F., Messner R., Weissinger E., Hayn M., Tomme P., Esterbauer H., Küchler E., Claeyssens M., Kubicek C. P. Monoclonal antibodies against different domains of cellobiohydrolase I and II from. Trichoderma reesei. Biochim. Biophys. Acta 1989; 990: 1
   PubMedGoogle Scholar
• Luderer M. E. H., Hofer F., Hagspiel K., Allmaier G., Blaas D., Kubicek C. P. A re-appraisal of multiplicity of endoglucanase I from Trichoderma reesei using monoclonal antibodies and plasma desorption mass spectrometry. Biochim. Biophys. Acta 1991; 1076: 427
   PubMedGoogle Scholar
• Hofer F., Weissinger E., Mischak H., Messner R., Meixner-Monori B., Blaas D., Visser J., Kubicek C. P. A monoclonal antibody against the alkaline extracellular β-glucosidase from Trichoderma reesei; reactivity with other Trichoderma β-glucosidases. Biochim. Biophys. Acta 1989; 992: 298
   Google Scholar
• Hagspiel K., Haab D., Kubicek C. P. Protease activity and proteolytic modifications of cellulases from a Trichoderma reesei QM 9414 selectant. Appl. Microbiol. Biotechnol. 1989; 32: 61
   Google Scholar
• Kolbe J., Kubicek C. P. Quantification and identification of the main components of the Trichoderma cellulase complex with monoclonal antibodies using an enzyme linked immunosorbent assay (ELISA). Appl. Microbiol. Biotechnol. 1990; 34: 26
   PubMed Web of Science ®Google Scholar
• Kubicek-Pranz E. M., Gsur A., Hayn M., Kubicek C. P. Characterization of commercial Trichoderma reesei cellulase preparations by denaturing electrophoresis (SDS-PAGE) and immunostaining using monoclonal antibodies. Biotechnol. Appl. Biochem. 1991; 14: 317
   PubMed Web of Science ®Google Scholar
• Seiboth B. The Role of Cellulases and β-Glucosidases in the Molecular Regulation of Cellulase Biosynthesis in Trichoderma reesei. Ph.D. thesis, TU Vienna 1995
   Google Scholar
• Stangl H., Gruber F., Kubicek C. P. Characterization of the Trichoderma reesei cbh2 promoter. Curr. Genet. 1993; 23: 115
   PubMed Web of Science ®Google Scholar
• Kubicek C. P., Messner R., Gruber F., Mach R. L., Kubicek-Pranz E. M. The Trichoderma cellulase regulatory puzzle: from the interior life of a secretory fungus. Enzyme Microb. Technol. 1993; 15: 90
   PubMed Web of Science ®Google Scholar
• Gamerith G., Groicher R., Zeilinger S., Herzog P., Kubicek C. P. Formation of cellulase-poor xylanases by Trichoderma reesei RUT C-30 on hemicellulose wastes from viscose fiber production. Appl. Microbiol. Biotechnol. 1992; 38: 315
   Web of Science ®Google Scholar
• Schrimpf S., Kulmitzer W., Latzko F., Kubicek C. P., Kubicek-Pranz E. M., Hampel W. Kinetics of xylanase formation by Trichoderma reesei on defined carbon substrates. 6th Eur. Conf. Biotechnol. Florence, Italy 1993, poster
   Google Scholar
• Gomes J., Gomes I., Steiner W., Esterbauer H. Production of cellulase and xylanase by a wild-strain of. Trichoderma viride. Appl. Microbiol. Biotechnol. 1992; 36: 701
   Web of Science ®Google Scholar
• Haltrich D., Preiss M., Steiner W. Optimization of a culture medium for increased xylanase production by a wild strain of. Schizophyllum commune. Enzyme Microb. Technol. 1993; 15: 10
   Google Scholar
• Haltrich D., Laussamayer B., Steiner W. Xylanase formation by Sclerotium rolfsii: effect of growth substrates and development of a culture medium using statistically designed experiments. Appl. Microbiol. Biotechnol. 1994; 42: 522
   Web of Science ®Google Scholar
• Purkarthofer H., Sinner M., Steiner W. Cellulase-free xylanase from Thermomyces lanuginosus: optimization of production in submerged and solid-state culture. Enzyme Microb. Technol. 1993; 15: 677
   Web of Science ®Google Scholar
• Gomes J., Gomes I., Kreiner W., Esterbauer H., Sinner M., Steiner W. Production of high level of cellulase-free and thermostable xylanase by a wild strain of Thermomyces lanuginosus using beechwood xylan. J. Biotechnol. 1993; 30: 283
   Google Scholar
• Gomes J., Purkarthofer H., Hayn M., Kapplmüller J., Sinner M., Steiner W. Production of a high level of cellulase-free xylanase by the thermophilic fungus Thermomyces lanuginosus in laboratory and pilot scales using lignocellulosic materials. Appl. Microbiol. Biotechnol. 1993; 39: 700
   Web of Science ®Google Scholar
• Purkarthofer H., Sinner M., Steiner W. Effect of shear rate and culture pH on the production of xylanase by. Thermomyces lanuginosus. Biotechnol. Lett. 1993; 15: 405
   Google Scholar
• Lischnig T., Purkarthofer H., Steiner W. Thermostability of endo-β-xylanase from the thermophilic fungus. Thermomyces lanuginosus. Biotechnol. Lett. 1993; 15: 411
   Google Scholar
• Sinner M., Ditzelmüller G., Witzani W., Steiner W. Biobleaching. Tree Cult. Proc. Util. 1991; 41: 1991
   Google Scholar
• Wizard W., Gomez J., Esterbauer H., Steiner W., Sinner M. Production of a cellulase-free xylanase and application. Lignocellulosics 1992; 101
   Google Scholar
• Kubicek C. P., Herzog P., Kristufek D., Hodits R., Kubicek-Pranz E. M., Messner R., Törrönen A., Harkki A. Interrelationships and differences in the regulation of xylanase and cellulase formation by Trichoderma reesei. Biotechnology in the Pulp and Paper Industry, M. Kuwahara, M. Shimada. Uni Publishing, TokyoJapan 1992; 383
   Google Scholar
• Kristufek D., Zeilinger S., Kubicek C. P. Regulation of β-xylosidase formation by xylose in. Trichoderma reesei. Appl. Microbiol. Biotechnol. 1995; 42: 713
   Google Scholar
• Arisan-Atac I., Hodits R., Kristufek D., Kubicek C. P. Purification and characterization of a β-mannanase from Trichoderma reesei RUT C-30. Appl. Microbiol. Biotechnol. 1993; 39: 58
   Web of Science ®Google Scholar
• Zeilinger S., Kristufek D., Arisan-Atac I., Hodits R., Kubicek C. P. Conditions for formation, purification and characterization of an α-galactosidase of Trichoderma reesei RUT C-30. Appl. Environ. Microbiol. 1993; 59: 1347
   PubMed Web of Science ®Google Scholar
• Kristufek D., Hodits R., Kubicek C. P. Coinduction of α-Al-arabinofuranosidase and α-d-galactosidase formation in Trichoderma reesei RUT C-30. FEMS Microbiol. Lett. 1994; 115: 259
   Web of Science ®Google Scholar
• Törrönen A., Mach R. L., Messner R., Gonzalez R., Kalkkinen N., Harkki A. M., Kubicek C. P. The two major xylanases of Trichoderma reesei: characterization of both proteins and genes. Biotechnology 1992; 10: 1461
   PubMedGoogle Scholar
• Törrönen A., Kubicek C. P., Henrissat B. Amino acid sequence similarities between low molecular weight endo-β-1,4-xylanases and family H cellulases revealed by clustering analysis. FEBS Lett. 1993; 321: 135
   PubMedGoogle Scholar
• Herrmann M., Vrsanska M., Biely P., Kubicek C. P. Characterization of a β-xylosidase from Trichoderma reesei. 6th Int. Conf. Biotechnology in the Pulp and Paper Industry. June. Vienna, Austria 1995, Abstract
   Google Scholar
• Herrmann M. The Xylanolytic Enzyme System of Trichoderma reesei: Activity Profile of the Xylanases, Identification of an Exo-β-1,4-xylanase and Cloning of its Gene. Ph.D. thesis, TU, Vienna 1995
   Google Scholar
• Hodits R., Butterweck A., Goller S. P., Törrönen A., Mach R. L., Messner R., Harkki A. M., Kubicek C. P. Recombinant Trichoderma reesei strains producing improved and “tailor” made xylanase profiles. ECB6: Proc. Sixth Eur. Cong. Biotechnol., L. Alberghina, L. Frontali, P. Sensi. Elsevier Science B. V., Amsterdam 1993; 295
   Google Scholar
• Biely P., Vrsanska M., Kremnicky L., Tenkanen M., Poutanen K., Hayn M. Catalytic properties of endo-β-1,4-xylanases of Trichoderma reesei. Proc. Second TRICEL Symp. Trichoderma reesei Cellulases and Other Hydrolytic Enzymes, P. Suominen, T. Reinikainen. Foundation of Biotechnical and Industrial Fermentation Research, EspooFinland 1993; 125
   Google Scholar
• Schall S., Ditzelmüller G., Steiner W., Hodits R., Kubicek C. P. Action of fungal hemicellulases on sulphite pulps. Tricel 93, Majvik, Finland 1993, Abstract
   Google Scholar
• Maringer U., Wong K. K. Y., Saddler J. N., Kubicek C. P. A functional comparison of two pairs of β-1,4-xylanases from Trichoderma harzianum E58 and Trichoderma reesei RUT C-30. Biotechnol. Appl. Biochem. 1995; 21: 49
   Google Scholar
• Mach R. L., Butterweck A., Schindler M., Messner R., Herzog P., Kubicek C. P. Molecular regulation of formation of xylanase (XYN) I and II by Trichoderma reesei. Proc. Second TRICEL Symp. Trichoderma reesei Celluloses and Other Hydrolytic Enzymes, P. Suominen, T. Reinikainen. Foundation of Biotechnical and Industrial Fermentation Research, EspooFinland 1993; 211
   Google Scholar
• Mach R. L., Strauss J., Schindler M., Zeilinger S., Adler G., Kubicek C. P. Glucose repression of xylanase formation by Trichoderma reesei regulates xyn1 but not xyn2 gene expression and is mediated by the Cre1 gene product. 18th Fungal Genet. Conf. Asilomar, 1995, poster II-14
   Google Scholar
• Lackner R., Srebotnik E., Messner K. Oxidative degradation of high molecular weight chlorolignin by manganese peroxidase of Phanerochaete chrysosporium. Biochem. Biophys. Res. Comm., 178: 1092–1098
   PubMedGoogle Scholar
• Srebotnik E., Messner K. Immunoelectron microscopical study of the porosity of brown-rot degraded pine wood. Holzforschung 1991; 45: 95
   Google Scholar
• Messner K., Masek S., Srebotnik E., Techt G. Fungal pretreatment of wood chips for chemical pulping. Proc. Fifth Int. Conf. Biotechnol. Pulp and Paper Industry, M. Kuwahara, M. Shimada. Uni Publishing, Tokyo 1992; 9
   Google Scholar
• Messner K., Srebotnik E. Biopulping: An overview of developments in an environmentally safe paper-making technology. FEMS Microbiol. Rev. 1994; 13: 351
   Web of Science ®Google Scholar
• Srebotnik E., Messner K. A simple method that uses differential staining and light microscopy to assess the selectivity of wood delignification by white rot fungi. Appl. Environ. Microbiol. 1994; 60: 1383
   PubMed Web of Science ®Google Scholar
• Latzko F., Strauss S., Hampel W. Formation of chitin degrading enzymes by Arthrobacter sp. — kinetic aspects. DECHEMA Biotechnol. Conf. 1992; 5: 177
   Google Scholar
• John E., Hampel W. A. Enzyme formation by a yeast cell wall lytic Arthrobacter species: formation of amylase. Appl. Microbiol. Biotechnol. 1992; 38: 214
   Google Scholar
• Werner L., Latzko F., Hampel W. A. Spray drying of yeast-lytic enzymes from Arthrobacter sp. Biotechnol. Technol. 1993; 7: 663
   Google Scholar
• Strauss S., Rauscher U., Zemanovic J., Hampel W. A. Formation of proteases by. Brevibacterium linens. DECHEMA Biotechnol. Conf. 1992; 5: 181
   Google Scholar
• Margesin R., Palma N., Knauseder F., Schinner F. Proteases of psychotrophic bacteria isolated from glaciers. J. Basic Microbiol. 1991; 31: 377
   Web of Science ®Google Scholar
• Margesin R., Palma N., Knauseder F., Schinner F. Purification and characterization of an alkaline serine protease produced by a psychotrophic Bacillus sp. J. Biotechnol. 1992; 24: 203
   Google Scholar
• Margesin R., Schinner F. Production and properties of an extracellular metalloprotease from a psychophilic. Pseudomonas fluorescens. J. Biotechnol. 1992; 24: 207
   Google Scholar
• Spok A., Stubenrauch G., Schörgendorfer K., Schwab H. Molecular cloning and sequencing of a pectinesterase gene from. Pseudomonas solanacearum. J. Gen. Microbiol. 1991; 137: 131
   PubMedGoogle Scholar
• Wanker E., Schörgendorfer K., Schwab H. Expression of the Bacillus subtilis le vanase gene in Escherichia coli and. Saccharomyces cerevisiae. J. Biotechnol. 1991; 18: 243
   PubMedGoogle Scholar
• Berger B., de Raadt A., Griengl H., Hayden W., Hechtberger P., Faber K. Useful hydrolytic enzymes: proteases, lipases and nitrilases. Pure Appl. Chem. 1992; 64: 1085
   Google Scholar
• Spreitz J., Grobbauer R., Griengl H., Faber K. Lipase-catalyzed resolution of bicyclic building blocks for leukotriene synthesis: advantages of organic media. Lipases Struct. Mech. Genet. Eng. 1991; 373
   Google Scholar
• De Raadt A., Klempier N., Faber K., Griengl H. Chemoselective enzymatic hydrolysis of aliphatic and alicyclic nitriles. J. Chem. Soc. Perkin Trans. 1992; 1992: 137
   Google Scholar
• De Raadt A., Griengl H., Klempier N., Suetz A. E. A mild and simple enzymatic conversion of aldono- and aldurononitriles into the corresponding amides and/or carboxylic acids. J. Org. Chem. 1993; 58: 3179
   Web of Science ®Google Scholar
• Fischer K., Messner K. Adsorption of lipase on pulp fibers during biological pitch control in paper industry. Enzyme Microb. Technol. 1992; 14: 470
   Google Scholar
• Fischer K., Puchinger L., Schloffer K., Kreiner W., Messner K. Enzymic pitch control of sulfite pulp on pilot scale. J. Biotechnol. 1993; 27: 341
   Web of Science ®Google Scholar
• Fischer K., Akhtar M., Blanchette R. A., Burnes T. A., Messner K., Kirk T. K. Reduction of resin content in wood chips during experimental biological pulping processes. Holzforschung 1994; 48: 285
   Google Scholar
• Fischer K., Messner K. Reducing troublesome pitch in pulp mills by lipolytic enzymes. Tappi J. 1992; 75: 130
   Web of Science ®Google Scholar
• Preitschopf W., Marr R. Enzyme immobilization in liquid surfactant membranes. DECHEMA Biotechnol. Conf. 1990; 4: 881
   Google Scholar
• Hawa G., Schalkhammer T., Mann-Buxbaum E., Pittner F. Ligand interaction based electrochemical glucose sensor. Sens. Actuators B 1993; 16: 423
   Google Scholar
• Burgstaller W., Schinner F. Leaching of metals with fungi. J. Biotechnol. 1992; 27: 91
   Google Scholar
• Strasser H., Pümpel T., Brunner H., Schinner F. Improvement of the quality of quartz sand by means of microbial leaching of iron oxide. Arch. Lagerstoffschg. Geol. B 1993; 16: 103
   Google Scholar
• Strasser H., Burgstaller W., Schinner F. High-yield production of oxalic acid for metal leaching processes by. Aspergillus niger. FEMS Microbiol. Lett. 1994; 119: 365
   PubMed Web of Science ®Google Scholar
• Burgstaller W., Strasser H., Woebking H., Schinner F. Solubilization of zinc oxide from filter dust with Penicillium simplicissimum: bioreactor leaching and stoichiometry. Environ. Sci. Technol. 1992; 26: 340
   Web of Science ®Google Scholar
• Franz A., Burgstaller W., Schinner F. Leaching with Penicillium simplicissimum: influence of metals and buffers on proton extrusion and citric acid production. Appl. Environ. Microbiol. 1991; 57: 769
   PubMed Web of Science ®Google Scholar
• Franz A., Burgstaller W., Müller B., Schinner F. Influence of medium components and metabolic inhibitors on citric acid production by. Penicillium simplicissimum. J. Gen. Microbiol. 1993; 139: 2101
   PubMedGoogle Scholar
• Wenzl R., Burgstaller W., Schinner F. Extraction of zinc, copper, and lead from a filter dust by yeast. Biorecovery 1990; 2: 1
   Google Scholar
• Puempel T., Schinner F. Native fungal pellets as a biosorbent for heavy metals. FEMS Microbiol. Rev. 1993; 11: 159
   Google Scholar
• Luef E., Prey T., Kubicek C. P. Zinc biosorption by fungal waste mycelia. Appl. Microbiol. Biotechnol. 1991; 34: 688
   Web of Science ®Google Scholar
• Ditzelmüller G., Loidl M., Streichsbier F. Isolation and characterization of a 2,4-dichlorophenoxyacetic acid degrading bacterium. Appl. Microbiol. Biotechnol. 1989; 31: 93
   Web of Science ®Google Scholar
• Loidl M., Hinteregger C., Ditzelmüller G., Ferschl A., Streichsbier F. Degradation of aniline and monochlorinated anilines by soil-borne Pseudomonas acidovorans strain. Arch. Microbiol. 1990; 155: 56
   Web of Science ®Google Scholar
• Ferschl A., Loidl M., Ditzelmüller G., Hinteregger C., Streichsbier F. Continuous degradation of 3-chloroaniline by calcium alginate entrapped cells of Pseudomonas acidovorans CA28: influence of additional substrates. Appl. Microbiol. Biotechnol. 1991; 35: 544
   Google Scholar
• Loidl M., Hinteregger C., Stockinger J., Ferschl A., Schein R., Streichsbier F. Degradation of o-. m, p-toluidine as pure substrates and mixtures by an isolated Pseudomonas wild-type strain. DECHEMA Biotechnol. Conf., 5: 1089
   Google Scholar
• Stockinger J., Hinteregger C., Loidl M., Ferschl A., Streichsbier F. Mineralization of 3-chloro-4-methylaniline via an ortho-cleavage pathway by Pseudomonas cepacia strain CMA1. Appl. Microbiol. Biotechnol. 1992; 38: 421
   Web of Science ®Google Scholar
• Hinteregger C., Loidl M., Streichsbier F. Characterization of isofunctional ring-cleavaging enzymes in aniline and 3-chloroaniline degradation by Pseudomonas acidovorans CA28. FEMS Microbiol. Lett. 1992; 97: 261
   Google Scholar
• Hinteregger C., Ferschl A., Loidl M., Streichsbier F. Metabolism of aniline and 3-chloroaniline in Pseudomonas acidovorans CA28: evidence of isofunctional muconate cycloisomerases. J. Basic Microbiol. 1993; 33: 301
   Google Scholar
• Hinteregger C., Leitner R., Loidl M., Ferschl A., Streichsbier F. Degradation of phenol and phenolic compounds by Pseudomonas putida EKII. Appl. Microbiol. Biotechnol. 1992; 37: 252
   PubMed Web of Science ®Google Scholar
• Plas C., Harant H., Danner H., Jelinek E., Wimmer K., Holubar P., Braun R. Ratio of biological and chemical oxidation during the aerobic elimination of sulphide by colourless sulphur bacteria. Appl. Microbiol. Biotechnol. 1992; 36: 817
   Web of Science ®Google Scholar
• Plas H., Wimmer K., Holubar P., Mattanovich D., Danner H., Jelinek E., Harant H., Braun R. Degradation of carbondisulphide by a Thiobacillus isolate. Appl. Microbiol. Biotechnol. 1993; 38: 820
   Google Scholar
• Bauer E., Pennerstorfer C., Holubar P., Plas C., Braun R. Microbial activity measurements in soil — a comparison of methods. J. Microbiol. Meth. 1991; 14: 109
   Google Scholar
• Kroiss H., Schweighofer P., Frey W., Matsche N. Nitrification inhibition — a source identification method for combined municipal and/or industrial wastewater treatment plants. Water Sci. Technol. 1992; 26: 1135
   Web of Science ®Google Scholar
• Nowak O., Schweighofer P., Svardal K. Nitrification inhibition — a method for the estimation of actual maximum autotrophic growth rates in activated sludge systems. Water Sci. Technol., in press
   Google Scholar
• Nowak O., Svardal K. Observations on the kinetics of nitrification under inhibiting conditions caused by industrial waste water compounds. Water Sci. Technol. 1993; 28: 115
   Web of Science ®Google Scholar
• Matsche N., Moser D. Operation of a two-stage activated sludge package plant for high efficiency treatment. Water Sci. Technol. 1993; 28: 299
   Web of Science ®Google Scholar
• Kroiss H., Svardal K., Novak O. Anaerobic-aerobic pretreatment of waste paper mill effluent. Water Sci. Technol. 1992; 25: 23
   Google Scholar
• da Camara Machado A., da Camaro Machado Laimer M. Genetic transformation in Prunus armeniaca L. (apricot). Biotechnology in Agriculture and Forestry, Plant Protoplasts and Genetic Engineering, Y. P. S. Bajaj, 1995, in press
   Google Scholar
• Laimer M., da Camara Machado A., Hanzer V., Himmler G., Mattanovich D., Katinger H. D. Regeneration of shoots from leaf discs of fruit trees as a tool for transformation. Acta Hort. 1989; 235: 85
   Google Scholar
• Mattanovich D., Rüker F., da Camara Machado A., Laimer M., Regner F., Steinkellner H., Himmler G., Katinger H. D. Efficient transformation of. Agrobacterium spp. by electroporation. Nucleic Acids Res. 1989; 17: 6747
   PubMed Web of Science ®Google Scholar
• Mattanovich D., Katinger H. W. The complete nucleotide sequence of plum pox virus RNA. J. Gen. Virol. 1989; 70: 513
   PubMedGoogle Scholar
• Himmler G., Frank S., Steinkellner H., Rüker F., Mattanovich D., Katinger H. Detection of the trans activity of the plum pox virus Nla-protease in infected plants. J. Gen. Virol. 1990; 71: 1623
   PubMedGoogle Scholar
• Mattanovich D., Himmler G., Laimer M., Maiss E., Regner F., da Camaro Machado A., Hanzer V., Casper R., Katinger H. Expression of the plum pox virus coat protein region in. Escherichia coli. Virus Genes 1989; 2: 119
   PubMedGoogle Scholar
• Steinkellner H., Himmler G., Sagl R., Mattanovich D., Katinger H. Amino-acid sequence comparison of nepovirus coat protein. Virus Genes 1992; 6: 197
   PubMedGoogle Scholar
• Steinkellner H., Himmler G., Mattanovich D., Katinger H. Nucleotide sequence of AMV-capsid protein gene. Nucleic Acids Res. 1990; 18: 7182
   PubMedGoogle Scholar
• Regner F., da Camara Machado A., da Camara Machado Laimer M., Steinkellner H., Mattanovich D., Hanzer V., Weiss H., Katinger H. D. Coat protein mediated resistance to plum pox virus in Nicotiana clevelandii and. benthamiana. Plant Cell Rep. 1992; 11: 30
   PubMed Web of Science ®Google Scholar
• Laimer M., da Camara Machado A., Mattanovich D., Regner F., Hanzer V., Steinkellner H., Durnlok B., Himmler G., Katinger H. D. Expression of plum pox virus coat protein in. Nicotiana clevelandii. Acta Hort. 1989; 280: 577
   Google Scholar
• da Camara Machado A., Regner F., Steinkellner H., Mattanovich D., Hanzer V., Weiss H., Laimer da Camara Machado M., Katinger H. D. Coat protein-mediated protection against plum pox virus. Acta Hort. 1992; 309: 203
   Google Scholar
• Korschineck I., Himmler G., Sagl R., Steinkellner H., Katinger H. A PCR membrane spot assay for the detection of plum pox virus RNA in bark of infected trees. J. Virol. Meth. 1991; 31: 139
   PubMed Web of Science ®Google Scholar
• Dimou D., D'Onghia A. M., da Camaro Machado Laimer M., Savino M. Occurrence of grapevine chrome mosaic nepovirus in Austria. J. Phytopathol. 1994, in press
   Google Scholar
• Striedner J., Czygan F. C., Braunegg G. Contributions to the biotechnological production of sweeteners from. Stevia rebaudiana Bertoni. I. A method for the serial analysis of diterpene glycosides by HPLC. Acta Biotechnol. 1991; 11: 495
   Google Scholar
• Striedner J., Gutjahr E., Czygan F. C., Braunegg G. Contributions to the biotechnological production of sweeteners from. Stevia rebaudiana Bertoni. II. Induction of stevioside accumulation in cell cultures by variation of the nutrient medium and the analysis of small amounts of stevioside. Acta Biotechnol. 1991; 11: 501
   Google Scholar
• Striedner J., Geissler S., Czygan F. C., Braunegg G. Contributions to the bio-technological production of sweeteners from. Stevia rebaudiana Bertoni. III. Accumulation of secondary metabolites by means of a precursor and by elucidation of cell cultures. Acta Biotechnol. 1991; 11: 505
   Google Scholar
• Messner K., Fleck V., Bürgel J. Stämme des Pilzes Trichoderma, daraus hergestelltes Fungizid, sowie Verfahren zu dessen Anwendung. European Patent. 1993, submitted
   Google Scholar
• Schlick A., Lieckfeldt E., Kuhls K., Börner T., Messner K. Fingerprinting reveals gamma-ray induced mutations in fungal DNA: implications for identification of patent strains of. Trichoderma harzianum. Curr. Genet. 1994; 26: 74
   PubMedGoogle Scholar
• Hayes C. K., Klemsdal S., Lorito M., DiPietro A., Peterbauer C. K., Nakas J. P., Tronsmo A., Harman G. E. Isolation and sequence of an endochitinase-encoding gene from a cDNA library of Trichoderma harzianum. Gene, 138: 143
   PubMedGoogle Scholar
• Peterbauer C. K. Cloning of Genes Encoding Chitinolytic Enzymes of the Biocontrol Fungus Trichoderma harzianum. Ph.D. thesis, TU, Vienna 1995
   Google Scholar
• Heidenreich E. J., Kubicek C. P. Sequence of the pyr4 gene encoding orotidine-5-phosphate decarboxylase from the biocontrol fungus. Trichoderma harzianum. Gene 1994; 147: 151
   PubMedGoogle Scholar
• Wang Y.-L. Physiological and Genetic Studies on the Mycoparasitic Fungus Trichoderma harzianum. Ph.D. thesis, TU, Vienna 1996
   Google Scholar
• Schirmböck M., Lorito M., Wang Y.-L., Hayes C. K., Arisan-Atac I., Scala F., Harman G. E., Kubicek C. P. Molecular mechanisms involved in biocontrol by Trichoderma harzianum: co-induction and synergism of hydrolytic enzymes and peptaibol antibiotics. Appl. Environ. Microbiol. 1994; 60: 4364
   PubMed Web of Science ®Google Scholar
• Arisan-Atac I., Heidenreich E., Kubicek C. P. Randomly amplified polymorphic DNA fingerprinting identifies subgroups of Trichoderma viride and other. Trichoderma sp. capable of chestnut blight biocontrol. FEMS Microbiol. Lett. 1995; 126: 249
   PubMed Web of Science ®Google Scholar
• Haudek S. B., Kreuzinger N., Podeu R., Göbi F., Gruber F., Kubicek C. P. Detection and identification of mycorrhizal fungi by the polymerase chain reaction. Ninth North Am. Conf. Mycorrhiza. August. Guelph, Canada 1993, poster
   Google Scholar
• Buchacher A., Predl R., Tauer C., Purtscher M., Gruber G., Heider R., Steindl F., Trkola A., Jungbauer A., Katinger H. Human monoclonal antibodies against gp41 and gp120 as potential agents for passive immunization. Vaccines 1992; 92: 191
   Google Scholar
• Rüker F., Mattanovich D., Liegl W., Katinger H. A simple and efficient procedure for electrofusion of animal cells. Stud. Biophys. 1987; 119: 81
   Google Scholar
• Kohl J., Rüker F., Himmler G., Razazi E., Katinger H. Cloning and expression of an HIV-1 specific single chain Fv region fused to Escherichia coli alkaline phosphatase. Ann. N.Y. Acad. Sci. 1991; 646: 106
   PubMedGoogle Scholar
• Rüker F., Ebert V., Kohl J., Steindl F., Riegler H., Katinger H. Expression of a human monoclonal anti-HIV-1 antibody in CHO-cells. Ann. N.Y. Acad. Sci. 1991; 646: 212
   PubMedGoogle Scholar
• Mattanovixh D., Weik R., Thim S., Kramer W., Bayer K., Katinger H. Optimization of recombinant gene expression in Escherichia coli. Ann. N.Y. Acad. Sci., in press
   Google Scholar
• Muster T., Steindl F., Purtscher M., Trkola A., Klima A., Himmler G., Rüker F., Katinger H. A conserved neutralizing epitope on gp41 on human immunodeficiency virus type 1. J. Virol. 1993; 67: 6642
   PubMed Web of Science ®Google Scholar
• Casale E., Wenisch E., He X.-M., Righetti P. G., Snyder R. S., Jungbauer A., Tauer C., Rüker F., Carter D. C. Crystallization of the Fab from human monoclonal antibody against gp41 of human immunodeficiency virus type I. J. Mol. Biol., 216: 511
   PubMedGoogle Scholar
• Jungbauer A., Steindl F., Grunow R., Porstmann T., Ernst W., Purtscher M., Reiter M., Tauer C., Wenisch E., Katinger H. Pilotproduktion von humanen monoklonalen Antikörpern gegen HIV-1. Z. Klin. Med. 1990; 45: 351
   Google Scholar
• Döpel S.-H., Porstmann T., Grunow R., Jungbauer A., Von Baehr R. Application of a human monoclonal antibody in a rapid competitive anti-HIV ELISA. J. Immunol. Meth. 1989; 116: 229
   PubMedGoogle Scholar
• Bayer K., Jungbauer A., Kramer W., Lettner H., Schönhofer W., Skias M., Steindl F., Taverner N., Uhl K. Humane rekombinante Superoxide-Dismutase. Bioengineering 1990; 6: 24
   Google Scholar
• Hohenwarter O., Schmatz C., Katinger H. Stability of von Willebrand factor secretion in different human endothelial hybrid cell lines. Cytotechnology 1992; 8: 31
   PubMed Web of Science ®Google Scholar
• Jungbauer A., Tauer C., Wenisch E., Steindl F., Purtscher M., Reiter M., Unterluggauer F., Buchacher A., Uhl K., Katinger H. Pilot scale production of a human monoclonal antibody against human immunodeficiency virus 1. J. Biochem. Biophys. Meth. 1989; 19: 223
   PubMedGoogle Scholar
• Jungbauer A., Lettner H. P. Chemical disinfection of chromatographic resins. I. Preliminary studies and microbial kinetics. BioPharm 1994; 7(5)46
   Google Scholar
• Jungbauer A., Lettner H. P. Chemical disinfection of chromatographic resins. II. In situ treatment of packed columns and long-term stability of resins. BioPharm 1994; 7(8)37
   Google Scholar
• Vorauer K., Skias M., Trkola A., Schulz P., Jungbauer A. Scale-up of recombinant protein purification by hydrophobic interaction chromatography. J. Chromatogr. 1992; 625: 33
   PubMedGoogle Scholar
• Steindl F., Jungbauer A., Wenisch E., Himmler G., Katinger H. Isoelectric precipitation and gel chromatography for purification of monoclonal IgM. Enzyme Microb. Technol. 1987; 9: 361
   Google Scholar
• Righetti P. G., Wenisch E., Jungbauer A., Katinger H., Faupel M. Preparative purification of human monoclonal antibody isoforms in a multicompartment electrolyser with immobiline membranes. J. Chromatogr. 1990; 500: 681
   PubMed Web of Science ®Google Scholar
• Jungbauer A., Unterluggauer F., Steindl F., Rüker F., Katinger H. Combination of Zetaprep mass ion exchange chromatography for the purification of high-purity monoclonal antibodies. J. Chromatogr. 1987; 397: 313
   PubMedGoogle Scholar
• Jungbauer A., Wenisch E. High-performance liquid chromatography and related methods in purification of monoclonal antibodies. Monoclonal Antibodies: Production and Application, A. R. Liss, 1989; 161
   Google Scholar
• Tauer C., Buchacher A., Jungbauer A. DNA clearance in protein A affinity chromatography. J. Biochem. Biophys. Meth. 1995, in press
   PubMedGoogle Scholar
• Jungbauer A., Uhl K., Schulz P., Tauer C., Gruber G., Steindl F., Buchacher A., Schoenhofer W., Unterluggauer F. Displacement effects in large-scale chromatography. Biotechnol. Bioeng. 1992; 39: 579
   PubMedGoogle Scholar
• Harant H., Wimmer K., Wenisch E., Strutzenberger K., Reiter M., Bluml G. Two-dimensional electrophoresis as a tool for control of quality and consistency in production systems using animal cells — application in animal cell culture quality control. Cytotechnology 1992; 8: 119
   PubMedGoogle Scholar
• Jungbauer A., Tauer C., Wenisch E., Uhl K., Brunner J., Purtscher M., Steindl F., Buchacher A. Isolation of isoproteins from monoclonal antibodies and recombinant proteins by chromatofocusing. J. Chromatogr. 1990; 512: 157
   PubMedGoogle Scholar
• Wenisch E., Reiter S., Hinger S., Steindl F., Tauer C., Jungbauer A., Katinger H., Righetti P. G. Shifts in isoelectric points between cellular and secreted antibodies as revealed by isoelectric focusing and immobilized pH gradients. Electrophoresis 1990; 11: 966
   PubMedGoogle Scholar
• Weigang F., Reiter M., Jungbauer A., Katinger H. High-performance liquid chromatographic determination of metabolic products for fermentation control of mammalian cell culture analysis of carbohydrates, organic acids and orthophosphate using refractive index and ultraviolet detectors. J. Chromatogr. 1989; 497: 59
   PubMedGoogle Scholar
• Heith J., Scheirer W., Hampel W. Data acquisition, control and optimization of a continuous fermentation with hybridomas. Biochem. Eng. 1991; 216
   Google Scholar
• Haigermoser C., Chen G. Q., Grohmann E., Hrabak O., Schwab H. Stability of r-microbes: stabilization of plasmid vectors by the partitioning function of broad host range plasmid RP4. J. Biotechnol. 1993; 28: 291
   PubMedGoogle Scholar
• Gerlitz M., Hrabak O., Schwab H. Partitioning of broad-host range plasmid RP4 is a complex system involving site-specific recombination. J. Bacteriol. 1990; 172: 6194
   PubMed Web of Science ®Google Scholar
• Eberl L., Kristensen C. S., Givskov M., Grohmann E., Gerlitz M., Schwab H. Analysis of the multimer resolution system encoded by the parCBA operon of broad-host range plasmid RP4. Mol. Microbiol. 1994; 12: 131
   PubMedGoogle Scholar
• Reisinger G. R., Tedin K., Bläsi U., Lubitz H. W. Development of a conditional suicide system for containment of bacteria and plasmids. J. Microb. Release, manuscript submitted
   Google Scholar
• Mach R. L., Schindler M., Kubicek C. P. Transformation of Trichoderma reesei based on hygromycin resistance using homologous expression signals. Curr. Genet. 1994; 25: 567
   PubMed Web of Science ®Google Scholar
• Schindler M., Mach R. L., Vollenhofer S. K., Gruber F., Hodits R., Visser J., De Graaff L., Kubicek C. P. Characterization of the pyruvate kinase-encoding gene (pki1) of. Trichoderma reesei. Gene 1993; 130: 271
   PubMedGoogle Scholar
• Weber G., Leitner E. Disruption of the cyclosporin synthetase gene of Tolypocladium niveum. Curr. Genet., 26: 461–467
   PubMedGoogle Scholar
• Ernst W. J., Grabherr R. M., Katinger H. Direct cloning into the Autographa californica nuclear polyhidrosis virus for generation of recombinant viruses. Nucleic Acids Res. 1991; 22: 2855
   Google Scholar
• Katinger H. W. D. Recent advances in large-scale animal cell technology. Nogeikagaku Kaishi 1992; 66: 1
   Google Scholar
• Bliem R., Konopitzky K., Katinger H. Industrial animal cell reactor systems: aspects of selection and evaluation. Adv. Biochem. Eng. Biotechnol. 1991; 44: 1
   PubMedGoogle Scholar
• Reiter M., Blüml G., Gaida T., Zach N., Unterluggauer F., Doblhoff-Dier O. Modular integrated fluidized bed bioreactor technology. Biotechnology 1991; 9: 1100
   PubMedGoogle Scholar
• Doblhoff-Dier O., Unterluggauer F., Huss S., Plail R., Katinger H. W. Pilot scale modular hard- and software concept for animal cell fermentation. Anim. Cell Technol. 1992; 393
   Google Scholar
• Reiter M., Zach N., Gaida T., Blüml G., Doblhoff-Dier O., Unterluggauer F. Oxygenation in fluidized bed bioreactors using the microsparging technique. Anim. Cell. Technol. 1992; 386
   Google Scholar
• Blüml G., Zach N., Reiter M., Gaida T., Katinger H., Rauschert B., Austrian Patent A1322/91
   Google Scholar
• Katzbauer B., Moser A., Narodoslawsky M. Lactic acid production in aqueous two-phase systems. Lactobacillus casei fermentation in two-phase system, coupled with conventional solvent extraction. DECHEMA Biotechnol. Conf. 1992; 5: 711
   Google Scholar
• Friedl A., Gapes R., Windsperger A., Schmidt A. Continuous product removal from alcohol fermentations using stripping, extraction, and pervaporation. Downstream Proc. Biotechnol. 1989; 2: 249
   Google Scholar
• Reisinger H., Marr R., Froeschl F., Hartl J. Supercritical fluid extraction, liquid membrane-permeation and salting out process as a means of separation for bioproducts. DECHEMA Biotechnol. Conf. 1990; 4: 1051
   Google Scholar
• Reisinger H., Marr R. Multicomponent-liquid membrane permeation of organic acid-lactic acid purification from fermentation broth using emulsion-liquid membrane. Chem. Eng. Technol. 1992; 15: 363
   Google Scholar
• Plicka A., Hampel W. A. Automation of fermentations with personal computers. Biochem. Eng. 1991; 389
   Google Scholar
• Schuster G., Hampel W. A. Determination of trace levels of transition metal ions in fermentation broth by ion-pair chromatography. Anal. Chim. Acta 1992; 258: 275
   Google Scholar
• Mayr B., Horvath P., Moser A. Engineering approach to mixing quantification in bioreactors. Bioproc. Eng. 1992; 8: 137
   Google Scholar
• Mayr B., Nagy E., Horvat P., Moser A. Modeling of mixing and simulation of its effect on glutamic acid fermentation. Chem. Biochem. Eng. 1993; Q7: 31
   Google Scholar
• Mayr B., Horvat P., Nagy E., Moser A. Mixing models applied to industrial batch bioreactors. Bioproc. Eng. 1993; 9: 1
   Google Scholar
• Moser A. Mixing in bioreactors — bioprocess engineering aspects — mathematical model. Eur. Cong. Biotechnol. 1990; 5: 782
   Google Scholar
• Bales V., Halama D., Moser A. Chemical processes and bioprocessing — relative merits and disadvantages of chemical processes and biotechnology. Chem. Biochem. Eng. 1993; Q7: 177
   Google Scholar
• Moser A. Bioprocess stimulation in practice: joint strategy with modelling and experiments according to the formal macroapproach. Chem. Biochem. Eng. 1993; Q7: 21
   Google Scholar
• Narodoslawsky M., Friedler F., Kiraly L., Altenburger H. J. SIMBIOS — a new simulation program for biotechnology with novel design. Chem. Biochem. Eng. 1993; Q7: 27
   Google Scholar
• Moser A. Ecological process engineering. New science and technology paradigm. Biotech. Forum Eur. 1991; 11: 644
   Google Scholar
• Moser A. Ecological reactor operation: multiple criteria design. Chem. Biochem. Eng. 1992; Q6: 153
   Google Scholar